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Titolo:
Bone morphogenetic protein-1 processes probiglycan
Autore:
Scott, IC; Imamura, Y; Pappano, WN; Troedel, JM; Recklies, AD; Roughley, PJ; Greenspan, DS;
Indirizzi:
Univ Wisconsin, Dept Pathol & Lab Med, Madison, WI 53706 USA Univ Wisconsin Madison WI USA 53706 thol & Lab Med, Madison, WI 53706 USA Univ Wisconsin, Dept Biomol Chem, Madison, WI 53706 USA Univ Wisconsin Madison WI USA 53706 pt Biomol Chem, Madison, WI 53706 USA Shriners Hosp Children, Joint Dis Lab, Montreal, PQ H3G 1A6, Canada Shriners Hosp Children Montreal PQ Canada H3G 1A6 eal, PQ H3G 1A6, Canada Shriners Hosp Children, Genet Unit, Montreal, PQ H3G 1A6, Canada Shriners Hosp Children Montreal PQ Canada H3G 1A6 eal, PQ H3G 1A6, Canada McGill Univ, Dept Surg, Montreal, PQ H3G 1A6, Canada McGill Univ MontrealPQ Canada H3G 1A6 Surg, Montreal, PQ H3G 1A6, Canada
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 39, volume: 275, anno: 2000,
pagine: 30504 - 30511
SICI:
0021-9258(20000929)275:39<30504:BMPPP>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROCOLLAGEN C-PROTEINASE; PROTEOGLYCAN-II DECORIN; MAMMALIAN TOLLOID-LIKE; GROWTH-FACTOR-BETA; DERMATAN SULFATE PROTEOGLYCANS; HUMAN ARTICULAR-CARTILAGE; COMPLETE CDNA CLONING; GENOMIC ORGANIZATION; TARGETED DISRUPTION; FIBROGENIC CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Greenspan, DS Univ Wisconsin, Dept Pathol & Lab Med, Madison, WI 53706 USAUniv Wisconsin Madison WI USA 53706 , Madison, WI 53706 USA
Citazione:
I.C. Scott et al., "Bone morphogenetic protein-1 processes probiglycan", J BIOL CHEM, 275(39), 2000, pp. 30504-30511

Abstract

Bone morphogenetic protein-1 (BMP-1) is a metalloprotease that plays important roles in regulating the deposition of fibrous extracellular matrix in vertebrates, including provision of the procollagen C-proteinase activity that processes the major fibrillar collagens I-III. Biglycan, a small leucine-rich proteoglycan, is a nonfibrillar extracellular matrix component with functions that include the positive regulation of bone formation. Biglycan is synthesized as a precursor with an NH2-terminal propeptide that is cleaved to yield the mature form found in vertebrate tissues. Here, we show thatBMP-1 cleaves probiglycan at a single site, removing the propeptide and producing a biglycan molecule with an NH2 terminus identical to that of the mature form found in tissues. BMP-1-related proteases mammalian Tolloid and mammalian Tolloid-like 1 (mTLL-1) are shown to have low but detectable levels of probiglycan-cleaving activity. Comparison shows that wild type mouse embryo fibroblasts (MEFs) produce only fully processed biglycan, whereas MEFs derived from embryos homozygous null for the Bmp1 gene, which encodes both BMP-1 and mammalian Tolloid, produce predominantly unprocessed probiglycan, and MEFs homozygous null for both the Bmp1 gene and the mTLL-1 gene Tll1 produce only unprocessed probiglycan. Thus, all detectable probiglycan-processing activity in MEFs is accounted for by the products of these two genes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/04/20 alle ore 23:00:21